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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Schistosoma japonicum and UniProt Accession P08515
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2.5.1.18 glutathione transferaseIUBMB Comments
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
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Word Map
- 2.5.1.18
- catalase
- dismutase
- sod
-
pull-down
- malondialdehyde
- carcinogenesis
-
detoxify
- hepatocytes
-
smoke
- isoenzymes
- cyp1a1
-
smoking
-
case-control
-
electrophilic
- epoxide
-
aquatic
- wistar
-
genotoxic
-
insecticide
-
chemopreventive
- gill
-
hepatocarcinogenesis
- acetylcholinesterase
-
polycyclic
-
pesticide
- hydroperoxide
-
thiobarbituric
-
hepatotoxicity
-
tbars
-
ache
-
albino
- metallothioneins
-
cigarette
-
benzoapyrene
- phenobarbital
-
drug-metabolizing
-
preneoplastic
-
alt
- aflatoxin
- gssg
-
hepatoprotective
- schistosoma
- comet
- carboxylesterase
- mussel
-
udp-glucuronosyltransferase
-
methylation-specific
- gsh-px
-
organophosphate
- drug development
- medicine
- cyp2d6
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Schistosoma japonicum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase X
-
-
-
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GST
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
glutathione S-transferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
mechanisms for formation of specific mono(glutathionyl) or bis(glutathionyl) conjugates
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aryl group transfer
aryl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
RX:glutathione R-transferase
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
CAS REGISTRY NUMBER
COMMENTARY
50812-37-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3,5-triacryloyl-1,3,5-triazinane + glutathione
L-gamma-glutamyl-S-[3-(3,5-diacryloyl-1,3,5-triazinan-1-yl)-3-oxopropyl]-L-cysteinylglycine
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
chloride + L-gamma-glutamyl-S-(2,4-dinitrophenyl)-L-cysteinylglycine
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
2-chloro-5-nitropyridine + glutathione
chloride + L-gamma-glutamyl-S-(5-nitropyridin-2-yl)-L-cysteinylglycine
-
-
-
-
?
7-oxabicyclo[4.1.0]heptan-2-one + glutathione
chloride + L-gamma-glutamyl-S-(6-oxocyclohex-1-en-1-yl)-L-cysteinylglycine
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
-
-
-
?
methyl 3-(4-methoxyphenyl)oxirane-2-carboxylate + glutathione
chloride + L-gamma-glutamyl-S-[2-hydroxy-3-methoxy-1-(4-methoxyphenyl)-3-oxopropyl]-L-cysteinylglycine
-
-
-
-
?
additional information
?
-
the enzyme is the major detoxification enzyme of Schistosoma japonicum, a pathogenic helminth causing schistosomiasis
-
-
?
additional information
?
-
-
the enzyme is the major detoxification enzyme of Schistosoma japonicum, a pathogenic helminth causing schistosomiasis
-
-
?
additional information
?
-
-
a primary pathway for metabolism of electrophilic compounds in Schistosoma japonicum involves glutathione S-transferase-catalyzed formation of glutathione conjugates, overview, production of nonenzymatic GSH conjugates with electrophilic substrates often overwhelms the activity of the enzyme, overview
-
-
?
additional information
?
-
no detectable activity with 1,2-dichloro-4-nitrobenzene, bromosulphthalein, and 1,2-epoxy-3-(4-nitrophenoxy) propane
-
-
?
additional information
?
-
-
GST as fusion expression partner enhances the solubility of recombinant proteins
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme is the major detoxification enzyme of Schistosoma japonicum, a pathogenic helminth causing schistosomiasis
-
-
?
additional information
?
-
-
the enzyme is the major detoxification enzyme of Schistosoma japonicum, a pathogenic helminth causing schistosomiasis
-
-
?
additional information
?
-
-
a primary pathway for metabolism of electrophilic compounds in Schistosoma japonicum involves glutathione S-transferase-catalyzed formation of glutathione conjugates, overview, production of nonenzymatic GSH conjugates with electrophilic substrates often overwhelms the activity of the enzyme, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
-
production of recombinant selenoproteins with internal selenocysteine residues in Escherichia coli. Introduction of a selenocysteine residue into the catalytic site of glutathione S-transferase is not sufficient to induce glutathione peroxidase activity in spite of a maintained glutathione-binding capacity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Amino-4-{[4-({4-chloro-6-[(2-sulfophenyl)amino]-1,3,5-triazin-2-yl}amino)-3-sulfophenyl]amino}-9,10-dioxo-9,10-dihydro-2-anthracenesulfonic acid
-
L-gamma-glutamyl-S-(2-hydroxy-5-nitrophenyl)-L-cysteinylglycine
-
nonenzymatically synthesized GSH conjugate
L-gamma-glutamyl-S-[(17beta)-17-hydroxy-17-methyl-3-oxoandrost-4-en-4-yl]-L-cysteinylglycine
-
nonenzymatically synthesized GSH conjugate
L-gamma-glutamyl-S-[1-(3-chlorophenyl)-2-hydroxyethyl]-L-cysteinylglycine
-
nonenzymatically synthesized GSH conjugate
L-gamma-glutamyl-S-[2-(4-nitrophenyl)-2-oxoethyl]-L-cysteinylglycine
-
nonenzymatically synthesized GSH conjugate
L-gamma-glutamyl-S-[2-(6-oxocyclohex-1-en-1-yl)ethyl]-L-cysteinylglycine
-
nonenzymatically synthesized GSH conjugate
L-gamma-glutamyl-S-[3-[4-(carboxymethoxy)-2,3-dichlorophenyl]-3-oxopropyl]-L-cysteinylglycine
-
nonenzymatically synthesized GSH conjugate
N5-[(1S)-2-[(carboxymethyl)amino]-1-(cyanomethyl)-2-oxoethyl]glutamine
-
-
[(3aR,5R,7aR)-3a,5-dihydroxy-7a-methyloctahydro-1H-inden-1-one]-succinyl-glutathione
-
-
[(3aR,5S,7aR)-3a,5-dihydroxy-7a-methyloctahydro-1H-inden-1-one]-aspartyl-glutathione
-
-
[(3aR,5S,7aR)-3a,5-dihydroxy-7a-methyloctahydro-1H-inden-1-one]-succinyl-glutathione
-
-
additional information
-
implementation of both structure-based drug design and the concept of polyvalency to discover a series of potent and unsymmetrical GST inhibitors, stoichiometry of one inhibitor molecule per GST monomer via isothermal titration calorimetric measurement, overview, molecular modeling
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of formation of specific mono(glutathionyl) or bis(glutathionyl) conjugates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
187
1-chloro-2,4-dinitrobenzene
-
4°C, 20 mM sodium phosphate buffer, pH 6.5, 0.5 mM glutathione
0.044
2-chloro-5-nitropyridine
-
25°C, 20 mM sodium phosphate buffer, pH 7.0, 0.5 mM glutathione
0.037
7-oxabicyclo[4.1.0]heptan-2-one
-
4°C, 20 mM sodium phosphate buffer, pH 6.5, 0.5 mM glutathione
39
L-gamma-glutamyl-S-[2-hydroxy-3-methoxy-1-(4-methoxyphenyl)-3-oxopropyl]-L-cysteinylglycine
-
25°C, 20 mM sodium phosphate buffer, pH 7.0, 0.5 mM glutathione
0.63
methyl 3-(4-methoxyphenyl)oxirane-2-carboxylate
-
25°C, 20 mM sodium phosphate buffer, pH 7.0, 0.5 mM glutathione
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.774
gamma-glutamyl-(c-methoxycarbonyl)-alpha-glutamylglycine
Schistosoma japonicum
-
pH 6.5, 30°C
0.00195
L-gamma-glutamyl-S-(2-hydroxy-5-nitrophenyl)-L-cysteinylglycine
Schistosoma japonicum
-
-
0.019
L-gamma-glutamyl-S-[(17beta)-17-hydroxy-17-methyl-3-oxoandrost-4-en-4-yl]-L-cysteinylglycine
Schistosoma japonicum
-
-
0.00096
L-gamma-glutamyl-S-[1-(3-chlorophenyl)-2-hydroxyethyl]-L-cysteinylglycine
Schistosoma japonicum
-
-
0.0755
L-gamma-glutamyl-S-[2-(4-nitrophenyl)-2-oxoethyl]-L-cysteinylglycine
Schistosoma japonicum
-
-
0.152
L-gamma-glutamyl-S-[2-(6-oxocyclohex-1-en-1-yl)ethyl]-L-cysteinylglycine
Schistosoma japonicum
-
-
0.000036
L-gamma-glutamyl-S-[3-[4-(carboxymethoxy)-2,3-dichlorophenyl]-3-oxopropyl]-L-cysteinylglycine
Schistosoma japonicum
-
-
0.147
N5-[(1S)-2-[(carboxymethyl)amino]-1-(cyanomethyl)-2-oxoethyl]glutamine
Schistosoma japonicum
-
pH 6.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GST26_SCHJA
218
0
25499
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structure analysis shows flexibility of the substrate-binding site
additional information
-
structure analysis shows flexibility of the substrate-binding site
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant GST-IRK, 10 mg/ml protein in 20 mM TrisHCl, pH 7.5, 150 mM NaCl, and 2 mM TCEP, 21°C, against 0.1 M Bis-Tris, pH 5.5, and 25% w/v PEG 3350, or 0.1 M sodium acetate pH 5.5, and 36% w/v PEG MME 5000 as precipitant solutions, 7 days, orthorhombic crystals, X-ray diffraction structure determination and analysis, at 3.0-3.14 A resolution, molecular-replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K44A
-
the mutant shows 95.9% binding affinity for GSH compared to the wild type enzyme
K44A/W40F
-
the mutant shows 95.2% binding affinity for GSH compared to the wild type enzyme
K44A/W40G
-
the mutant shows 65.7% binding affinity for GSH compared to the wild type enzyme
K44G
-
the mutant shows 97% binding affinity for GSH compared to the wild type enzyme
K44G/W40A/R41A
-
the mutant shows 49.3% binding affinity for GSH compared to the wild type enzyme
K44S
-
the mutant shows 95.6% binding affinity for GSH compared to the wild type enzyme
K44S/W40F/R41A
-
the mutant shows 66.2% binding affinity for GSH compared to the wild type enzyme
R41A
-
the mutant shows 97.5% binding affinity for GSH compared to the wild type enzyme
R41H
-
the mutant shows 99.55% binding affinity for GSH compared to the wild type enzyme
W40A
-
the mutant shows 89.7% binding affinity for GSH compared to the wild type enzyme
W40F
-
the mutant shows 96.7% binding affinity for GSH compared to the wild type enzyme
W40G
-
the mutant shows 81.1% binding affinity for GSH compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
irreversible inactivation, detailed thermal inactivation kinetics in presence or absence of glutathione and S-hexylglutathione, thermal unfolding at pH 6.5-8.5, pH-dependence, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
constitutive gst gene, expression of the enzyme as fusion protein with the full-length intracellular domain of the human insulin receptor, i.e. GST-IRK, comprising the coding region of IRK, residues Val966Lys1271, C969S, Y972F, and containing a thrombin-cleavage site as a linker between GSTand IRK, in Spodoptera frugiperda Sf9 cells
Expression of recombinant proteins with glutathione S-transferase as fusion expression partner in Escherichia coli strain BL21 (DE3).
-
production of recombinant selenoproteins with internal selenocysteine residues in Escherichia col, introduction of a variant bacterial-type selenocysteine insertion sequence element which afforded substitution with selenocysteine for the catalytic Tyr residue in the active site of the enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
commercial fusion partner using for enhancing the solubility of recombinant proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ortiz-Salmeron, E.; Yassin, Z.; Clemente-Jimenez, M.J.; Heras-Vazquez, F.J.L.; Rodriguez-Vico, F.; Baron, C.; Garcia-Fuentes, L.
Thermodynamic analysis of the binding of glutathione to glutathione S-transferase over a range of termeratures
Eur. J. Biochem.
268
4307-4314
2001
Schistosoma japonicum
Jiang, Z.; Arner, E.S.J.; Mu, Y.; Johansson, L.; Shi, J.; Zhao, S.; Liu, S.; Wang, R.; Zhang, T.; Yan, G.; Liu, J.; Shen, J.; Luo, G.
Expression of selenocysteine-containing glutathione S-transferase in Escherichia coli
Biochem. Biophys. Res. Commun.
321
94-101
2004
Schistosoma japonicum
Rufer, A.C.; Thiebach, L.; Baer, K.; Klein, H.W.; Hennig, M.
X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site
Acta Crystallogr. Sect. F
61
263-265
2005
Schistosoma japonicum (P08515), Schistosoma japonicum
Quesada-Soriano, I.; Garcia-Maroto, F.; Garcia-Fuentes, L.
Kinetic study on the irreversible thermal denaturation of Schistosoma japonicum glutathione S-transferase
Biochim. Biophys. Acta
1764
979-984
2006
Schistosoma japonicum
Lo, W.J.; Chiou, Y.C.; Hsu, Y.T.; Lam, W.S.; Chang, M.Y.; Jao, S.C.; Li, W.S.
Enzymatic and nonenzymatic synthesis of glutathione conjugates: application to the understanding of a parasites defense system and alternative to the discovery of potent glutathione S-transferase inhibitors
Bioconjug. Chem.
18
109-120
2007
Schistosoma japonicum
Jao, S.C.; Chen, J.; Yang, K.; Li, W.S.
Design of potent inhibitors for Schistosoma japonica glutathione S-transferase
Bioorg. Med. Chem.
14
304-318
2006
Schistosoma japonicum
Torres-Rivera, A.; Landa, A.
Glutathione transferases from parasites: a biochemical view
Acta Trop.
105
99-112
2008
Homo sapiens, Echinococcus granulosus (O16058), Rattus norvegicus (P04905), Schistosoma mansoni (P15964), Mus musculus (P24472), Schistosoma japonicum (P26624), Onchocerca volvulus (P46427), Ascaris suum (P46436), Fasciola hepatica (P56598), Sus scrofa (P80031), Clonorchis sinensis (Q1L2C7), Taenia solium (Q3ZJN3), Ancylostoma caninum (Q6J1M5), Plasmodium yoelii (Q7REH6), Wuchereria bancrofti (Q86LL8), Plasmodium falciparum (Q8MU52)
Park, J.S.; Han, K.Y.; Lee, J.H.; Song, J.A.; Ahn, K.Y.; Seo, H.S.; Sim, S.J.; Kim, S.W.; Lee, J.
Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive Escherichia coli protein, RpoS
BMC Biotechnol.
8
15
2008
Schistosoma japonicum
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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